NMR structure of human erythropoietin and a comparison with its receptor bound confor
 

NMR structure of human erythropoietin and a comparison with its receptor bound conformation.

Related Articles NMR structure of human erythropoietin and a comparison with its receptor bound conformation.

Nat Struct Biol. 1998 Oct;5(10):861-6

Authors: Cheetham JC, Smith DM, Aoki KH, Stevenson JL, Hoeffel TJ, Syed RS, Egrie J, Harvey TS

The solution structure of human erythropoietin (EPO) has been determined by nuclear magnetic resonance spectroscopy and the overall topology of the protein is revealed as a novel combination of features taken from both the long-chain and short-chain families of hematopoietic growth factors. Using the structure and data from mutagenesis studies we have elucidated the key physiochemical properties defining each of the two receptor binding sites on the EPO protein. A comparison of the NMR structure of the free EPO ligand to the receptor bound form, determined by X-ray crystallography, reveals conformational changes that may accompany receptor binding.

PMID: 9783743 [PubMed - indexed for MEDLINE]



Source: PubMed